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NPR1_ORYSI
ID   NPR1_ORYSI              Reviewed;         582 AA.
AC   Q5D0W8; B8ADQ5;
DT   07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=BTB/POZ domain and ankyrin repeat-containing protein NPR1 {ECO:0000305};
DE            Short=OsNPR1 {ECO:0000303|Ref.2};
DE   AltName: Full=NPR1 homolog 1 {ECO:0000305};
DE            Short=OsNH1 {ECO:0000303|PubMed:15986920};
GN   Name=NPR1 {ECO:0000303|Ref.2}; Synonyms=NH1 {ECO:0000303|PubMed:15986920};
GN   ORFNames=OsI_00749 {ECO:0000312|EMBL:EEC70102.1};
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH TGA2.2, AND
RP   MUTAGENESIS OF CYS-150 AND HIS-338.
RC   STRAIN=cv. IRBB21;
RX   PubMed=15986920; DOI=10.1094/mpmi-18-0511;
RA   Chern M., Fitzgerald H.A., Canlas P.E., Navarre D.A., Ronald P.C.;
RT   "Overexpression of a rice NPR1 homolog leads to constitutive activation of
RT   defense response and hypersensitivity to light.";
RL   Mol. Plant Microbe Interact. 18:511-520(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND FUNCTION.
RC   STRAIN=cv. Gui99;
RX   DOI=10.1007/s10658-011-9801-7;
RA   Feng J.X., Cao L., Li J., Duan C.J., Luo X.M., Le N., Wei H.H., Liang S.J.,
RA   Chu C.C., Pan Q.H., Tang J.L.;
RT   "Involvement of OsNPR1/NH1 in rice basal resistance to blast fungus
RT   Magnaporthe oryzae.";
RL   Eur. J. Plant Pathol. 131:221-235(2011).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [4]
RP   INTERACTION WITH NRR.
RX   PubMed=16115061; DOI=10.1111/j.1365-313x.2005.02485.x;
RA   Chern M., Canlas P.E., Fitzgerald H.A., Ronald P.C.;
RT   "Rice NRR, a negative regulator of disease resistance, interacts with
RT   Arabidopsis NPR1 and rice NH1.";
RL   Plant J. 43:623-635(2005).
CC   -!- FUNCTION: Key positive factor of disease resistance (PubMed:15986920,
CC       Ref.2). Involved in defense response against the bacterial blight
CC       disease caused by Xanthomonas oryzae pv. oryzae (Xoo). Plants over-
CC       expressing NPR1/NH1 acquire high levels of resistance to Xoo, express
CC       constitutively defense genes and develop lesion-mimic spots on leaves
CC       at pre-flowering stage (PubMed:15986920). Involved in basal resistance
CC       to the blast pathogen Magnaporthe oryzae. Plants over-expressing
CC       NPR1/NH1 have increased resistance to M.oryzae infection (Ref.2). Plays
CC       an essential role in benzothiadiazole (BTH)-induced resistance to the
CC       blast fungus disease caused by Magnaporthe oryzae (By similarity).
CC       Functions as a transcriptional coactivator of TGA2.1 and LG2 in vitro
CC       (By similarity). Involved in defense response against herbivore. Plants
CC       silencing NPR1/NH1 have increased herbivore-induced trypsin proteinase
CC       inhibitors and volatiles, which reduces the performance of the striped
CC       stem borer (SSB) Chilo suppressalis (By similarity).
CC       {ECO:0000250|UniProtKB:Q9FDY4, ECO:0000269|PubMed:15986920,
CC       ECO:0000269|Ref.2}.
CC   -!- SUBUNIT: Oligomer in an uninduced state; disulfide-linked. Forms
CC       activated monomer upon changes in cellular redox potential (By
CC       similarity). Interacts with TGA2.2 (Ref.2). Interacts with NRR
CC       (PubMed:16115061). {ECO:0000250|UniProtKB:Q9FDY4,
CC       ECO:0000269|PubMed:16115061, ECO:0000269|Ref.2}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus
CC       {ECO:0000250|UniProtKB:Q9FDY4}. Note=Accumulation in nucleus when
CC       present as monomer. {ECO:0000250|UniProtKB:Q9FDY4}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EEC70102.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY923983; AAX18700.1; -; mRNA.
DR   EMBL; GU722159; ADE05560.1; -; Genomic_DNA.
DR   EMBL; GU722160; ADE05561.1; -; mRNA.
DR   EMBL; CM000126; EEC70102.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q5D0W8; -.
DR   SMR; Q5D0W8; -.
DR   STRING; 39946.Q5D0W8; -.
DR   Proteomes; UP000007015; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:2000022; P:regulation of jasmonic acid mediated signaling pathway; IEA:InterPro.
DR   GO; GO:2000031; P:regulation of salicylic acid mediated signaling pathway; IEA:InterPro.
DR   GO; GO:0009862; P:systemic acquired resistance, salicylic acid mediated signaling pathway; IEA:InterPro.
DR   Gene3D; 1.25.40.20; -; 1.
DR   Gene3D; 3.30.710.10; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR044292; NPR.
DR   InterPro; IPR021094; NPR1/NIM1-like_C.
DR   InterPro; IPR024228; NPR_central_dom.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   PANTHER; PTHR46475; PTHR46475; 1.
DR   Pfam; PF13637; Ank_4; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF11900; DUF3420; 1.
DR   Pfam; PF12313; NPR1_like_C; 1.
DR   SMART; SM00248; ANK; 3.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS50097; BTB; 1.
PE   1: Evidence at protein level;
KW   ANK repeat; Cytoplasm; Disulfide bond; Nucleus; Plant defense;
KW   Reference proteome; Repeat.
FT   CHAIN           1..582
FT                   /note="BTB/POZ domain and ankyrin repeat-containing protein
FT                   NPR1"
FT                   /id="PRO_0000436999"
FT   DOMAIN          55..140
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   REPEAT          269..299
FT                   /note="ANK 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          301..328
FT                   /note="ANK 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          332..361
FT                   /note="ANK 3"
FT                   /evidence="ECO:0000255"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          525..544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          551..582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        565..582
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        76
FT                   /note="Interchain (with C-216); in linked form"
FT                   /evidence="ECO:0000250|UniProtKB:P93002"
FT   DISULFID        216
FT                   /note="Interchain (with C-76); in linked form"
FT                   /evidence="ECO:0000250|UniProtKB:P93002"
FT   MUTAGEN         150
FT                   /note="C->Y: Abolishes the interaction with TGA2.2."
FT                   /evidence="ECO:0000269|PubMed:15986920"
FT   MUTAGEN         338
FT                   /note="H->Y: Abolishes the interaction with TGA2.2."
FT                   /evidence="ECO:0000269|PubMed:15986920"
SQ   SEQUENCE   582 AA;  63897 MW;  E895DAB994D309F1 CRC64;
     MEPPTSHVTN AFSDSDSASV EEGDADADAD VEALRRLSDN LAAAFRSPED FAFLADARIA
     VPGGGGGGGD LRVHRCVLSA RSPFLRGVFA RRAAAAAGGG GEDGSERLEL RELLGGGGEE
     VEVGYEALRL VLDYLYSGRV GDLPKAACLC VDEDCAHVGC HPAVAFMAQV LFAASTFQVA
     ELTNLFQRRL LDVLDKVEVD NLLLILSVAN LCNKSCMKLL ERCLDMVVRS NLDMITLEKS
     LPPDVIKQII DARLSLGLIS PENKGFPNKH VRRIHRALDS DDVELVRMLL TEGQTNLDDA
     FALHYAVEHC DSKITTELLD LALADVNHRN PRGYTVLHIA ARRREPKIIV SLLTKGARPA
     DVTFDGRKAV QISKRLTKQG DYFGVTEEGK PSPKDRLCIE ILEQAERRDP QLGEASVSLA
     MAGESLRGRL LYLENRVALA RIMFPMEARV AMDIAQVDGT LEFNLGSGAN PPPERQRTTV
     DLNESPFIMK EEHLARMTAL SKTVELGKRF FPRCSNVLDK IMDDETDPVS LGRDTSAEKR
     KRFHDLQDVL QKAFHEDKEE NDRSGLSSSS SSTSIGAIRP RR
 
 
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